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Fig. 2. Characterization of the dLBR protein. (A-C) Total larval proteins of Drosophila melanogaster second (A, lane 1) and third (A, lane 2; B, lane 1) instar, and pupa (B, lane 2) were separated by SDS-PAGE and immunoblotted with affinity-purified dLBR antibodies (A) or non-purified dLBR antibodies (B,C). In each lane, total proteins of one animal were loaded. (C) Aliquots of S2 cells were incubated with 8 M urea and fractionated by 100,000 g centrifugation into a supernatant (S) and a pellet containing predominantly membranes (P). Proportional amounts of proteins of both fractions were separated by SDS-PAGE and immunoblotted with dLBR antibodies. A polypeptide of Mr 66,000 is detected by the dLBR antibodies (A-C, arrowheads). dLBR does form aggregates in SDS sample buffer resulting in a smear close to the top of the gel (A-C; Fig. 7A, Fig. 8A). Molecular masses of reference proteins (in kDa) are marked.





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